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6PGL_BUCAP
ID   6PGL_BUCAP              Reviewed;         333 AA.
AC   Q8K9N9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=6-phosphogluconolactonase {ECO:0000255|HAMAP-Rule:MF_01605};
DE            Short=6-P-gluconolactonase {ECO:0000255|HAMAP-Rule:MF_01605};
DE            EC=3.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01605};
GN   Name=pgl {ECO:0000255|HAMAP-Rule:MF_01605}; OrderedLocusNames=BUsg_282;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC       phosphogluconate. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC         + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01605};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- SIMILARITY: Belongs to the cycloisomerase 2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01605}.
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DR   EMBL; AE013218; AAM67839.1; -; Genomic_DNA.
DR   RefSeq; WP_011053806.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9N9; -.
DR   SMR; Q8K9N9; -.
DR   STRING; 198804.BUsg_282; -.
DR   EnsemblBacteria; AAM67839; AAM67839; BUsg_282.
DR   KEGG; bas:BUsg_282; -.
DR   eggNOG; COG2706; Bacteria.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   OMA; EGNWPRD; -.
DR   OrthoDB; 302683at2; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_01605; 6P_gluconolactonase; 1.
DR   InterPro; IPR022528; 6-phosphogluconolactonase_YbhE.
DR   InterPro; IPR019405; Lactonase_7-beta_prop.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF10282; Lactonase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT   CHAIN           1..333
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_0000171129"
SQ   SEQUENCE   333 AA;  38373 MW;  7D6B61FAEC29855C CRC64;
     MQQIIYIANA ESENIEVWIL YNNGDMKLIQ TVQTDGQVQP ISIIKNTKLL YAGIRPKNRV
     ITYQIDKNGL LKKKKESIVP GTPNYISFDS SEKFLFCSSY HADCISVSPL DKNGIPKDPI
     QIIHNIEGCH AAKFNSKYNV LFITSLKNDC IYLYYLTHFG ILKSTEQKLV FSQKNSGPRH
     VIFHPNQNFS YTVNELNGSV DVWKISKENK VLEVKNIQNI KLLNDLISKK YWSSDIHLTS
     CGNFLYVSDR YLNSISLFHV NKNDNTIIFF KQYLTEEQPR AFCIDRNNNY LIVIGQKSNK
     LSVYKICQKT GELKKINQYQ TGNGPLWITS FLI
 
 
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